This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-alanine:NAD+ oxidoreductase (deaminating). Other names in common use include AlaDH, L-alanine dehydrogenase, NAD+-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD+-dependent alanine dehydrogenase, alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. T
Respiratory complex I, EC 7.1.1.2 is the first large protein complex of the respiratory chains of many organisms from bacteria to humans. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and translocates protons across the inner mitochondrial membrane in eukaryotes or the plasma membrane of bacteria.
Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD+ to NADH. This reaction is part of many metabolic pathways, including the citric acid cycle. Other malate dehydrogenases, which have other EC numbers and catalyze other reactions oxidizing malate, have qualified names like malate dehydrogenase (NADP+).
Nitrate reductase (NADH) (EC 1.7.1.1, assimilatory nitrate reductase, NADH-nitrate reductase, NADH-dependent nitrate reductase, assimilatory NADH: nitrate reductase, nitrate reductase (NADH2), NADH2:nitrate oxidoreductase) is an enzyme with systematic name nitrite:NAD+ oxidoreductase. This enzyme catalyzes the following chemical reaction
In enzymology, a strombine dehydrogenase (EC 1.5.1.22) is an enzyme that catalyzes the chemical reaction
In enzymology, a (R,R)-butanediol dehydrogenase (EC 1.1.1.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a glucose 1-dehydrogenase (NAD+) (EC 1.1.1.118) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-arabinitol 2-dehydrogenase (EC 1.1.1.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a quinate dehydrogenase (EC 1.1.1.24) is an enzyme that catalyzes the chemical reaction
In enzymology, a ribitol-5-phosphate 2-dehydrogenase (EC 1.1.1.137) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction
In enzymology, a 7alpha-hydroxysteroid dehydrogenase (EC 1.1.1.159) is an enzyme that catalyzes the chemical reaction
In enzymology, a (S,S)-butanediol dehydrogenase (EC 1.1.1.76) is an enzyme that catalyzes the chemical reaction
In enzymology, an aldehyde dehydrogenase (NAD+) (EC 1.2.1.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a malonate-semialdehyde dehydrogenase (EC 1.2.1.15) is an enzyme that catalyzes the chemical reaction
Alanopine dehydrogenase (EC 1.5.1.17) is an enzyme that catalyzes the chemical reaction
In enzymology, a hypotaurine dehydrogenase (EC 1.8.1.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) is an enzyme that catalyzes the chemical reaction
L-2-hydroxycarboxylate dehydrogenase (NAD+) (EC 1.1.1.337, (R)-sulfolactate:NAD+ oxidoreductase, L-sulfolactate dehydrogenase, (R)-sulfolactate dehydrogenase, L-2-hydroxyacid dehydrogenase (NAD+), ComC) is an enzyme with systematic name (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
Pyruvate dehydrogenase (quinone) (EC 1.2.5.1, pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, pyruvate oxidase (ambiguous)) is an enzyme with systematic name pyruvate:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reaction
NADH dehydrogenase is an enzyme that converts nicotinamide adenine dinucleotide (NAD) from its reduced form (NADH) to its oxidized form (NAD+). Members of the NADH dehydrogenase family and analogues are commonly systematically named using the format NADH:acceptor oxidoreductase. The chemical reaction these enzymes catalyze is generally represented with the following equation:
↑ Tripathi SM, Ramachandran R (2008). "Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations". Proteins. 72 (3): 1089–95. doi:10.1002/prot.22101. PMID18491387. S2CID23999004.
Further reading
O'Connor RJ, Halvorson H (March 1961). "The substrate specificity of L-alanine dehydrogenase". Biochimica et Biophysica Acta. 48 (1): 47–55. doi:10.1016/0006-3002(61)90513-3. PMID13730044.
Yoshida A, Freese E (February 1965). "Enzymic properties of alanine dehydrogenase of Bacillus subtilis". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation. 96 (2): 248–62. doi:10.1016/0926-6593(65)90009-3. PMID14298830.
Tripathi SM, Ramachandran R (August 2008). "Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations". Proteins. 72 (3): 1089–95. doi:10.1002/prot.22101. PMID18491387. S2CID23999004.
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